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Competitive Adsorption of Lung Surfactant and Serum Proteins at the Air-Liquid Interface: A Grazing Incidence X-Ray Diffraction Study

Published online by Cambridge University Press:  01 February 2011

Patrick C Stenger ,
Guohui H Wu ,
Eva Y Chi ,
Shelli L Frey ,
Ka Yee C Lee ,
Jaroslaw Majewski ,
Kristian Kjaer  and
Joseph A Zasadzinski
Patrick C Stenger
Affiliation:
psteng@engineering.ucsb.edu, University of California, Santa Barbara, Department of Chemical Engineering, Engineering 2, Room 3357, Santa Barbara, CA, 93106-5080, United States
Guohui H Wu
Affiliation:
guohuiwu@engineering.ucsb.edu, University of California, Department of Chemical Engineering, Santa Barbara, CA, 93106-5080, United States
Eva Y Chi
Affiliation:
yunghuachi@yahoo.com, the University of Chicago, Chicago, IL, 60637, United States
Shelli L Frey
Affiliation:
sfrey@uchicago.edu, the University of Chicago, Chicago, IL, 60637, United States
Ka Yee C Lee
Affiliation:
kayeelee@uchicago.edu, the University of Chicago, Chicago, IL, 60637, United States
Jaroslaw Majewski
Affiliation:
jarek@lanl.gov, Los Alamos National Laboratory, Los Alamos, NM, 87545, United States
Kristian Kjaer
Affiliation:
Kristian.Kjaer@nbi.ku.dk, Risø National Laboratory, Roskilde, N/A, Denmark
Joseph A Zasadzinski
Affiliation:
gorilla@engineering.ucsb.edu, University of California, Department of Chemical Engineering, Santa Barbara, CA, 93106-5080, United States
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Abstract

The competitive adsorption of lung surfactant (LS) and albumin at the air-liquid interface and the ability of polyethylene glycol (PEG) to mediate LS adsorption are analyzed using pressure area isotherms and grazing incidence x-ray diffraction (GIXD). The addition of albumin drastically reduces the amount of LS on the interface and slightly increases the LS lattice spacing. The addition of PEG restores the characteristic LS peaks, yielding a slightly more compact lattice. The scattering results are consistent with recent work which proposed that albumin creates a physical barrier which eliminates LS adsorption and that PEG enhances LS adsorption but does not significantly change LS surface ordering.

Keywords

x-ray diffraction (XRD)adsorptionbiomedical
Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 1027: Symposium D – Materials in Transition–Insights from Synchrotron and Neutron Sources , 2007 , 1027-D05-09
Copyright
Copyright © Materials Research Society 2008

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